Structure of thermotoga maritima stationary phase survival protein SurE : a novel acid phosphatase.
Background: The rpoS, nlpD, pcm, and surE genes are among many whose expression is induced during the stationary phase of bacterial growth. rpoS codes for the stationary-phase RNA polymerase {sigma} subunit, and nlpD codes for a lipoprotein. The pcm gene product repairs damaged proteins by converting the atypical isoaspartyl residues back to L-aspartyls. The physiological and biochemical functions of surE are unknown, but its importance in stress is supported by the duplication of the surE gene in E. coli subjected to high-temperature growth. The pcm and surE genes are highly conserved in bacteria, archaea, and plants. Results: The structure of SurE from Thermotoga maritima was determined at 2.0 Angstroms. The SurE monomer is composed of two domains; a conserved N-terminal domain, a Rossman fold, and a C-terminal oligomerization domain, a new fold. Monomers form a dimer that assembles into a tetramer. Biochemical analysis suggests that SurE is an acid phosphatase, with an optimum pH of 5.5-6.2. The active site was identified in the N-terminal domain through analysis of conserved residues. Structure-based site-directed point mutations abolished phosphatase activity. T. maritima SurE intra- and intersubunit salt bridges were identified that may explain the SurE thermostability. Conclusions: The structure of SurE provided information about the protein's fold, oligomeric state, and active site. The protein possessed magnesium-dependent acid phosphatase activity, but the physiologically relevant substrate(s) remains to be identified. The importance of three of the assigned active site residues in catalysis was confirmed by site-directed mutagenesis.
- Research Organization:
- Argonne National Laboratory (ANL)
- Sponsoring Organization:
- SC
- DOE Contract Number:
- AC02-06CH11357
- OSTI ID:
- 949307
- Report Number(s):
- ANL/BIO/JA-39803
- Journal Information:
- Structure, Journal Name: Structure Journal Issue: 11 ; Nov. 2001 Vol. 9
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Structures of and Interactions Between Domains of Trigger Factor from Thermotoga maritima
The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.
Crystal structure of Thermotoga maritima 0065 - a member of the IclR transcriptional factor family
Journal Article
·
Sun Dec 31 23:00:00 EST 2006
· Acta Crystallographica Section D: Biological Crystallography
·
OSTI ID:930395
The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.
Journal Article
·
Mon Dec 31 23:00:00 EST 2001
· Nature Struct. Biol.
·
OSTI ID:949508
Crystal structure of Thermotoga maritima 0065 - a member of the IclR transcriptional factor family
Journal Article
·
Fri May 24 00:00:00 EDT 2002
· J. Biol. Chem.
·
OSTI ID:949514